5td4

Starch binding sites on the Human pancreatic alpha amylase D300N variant complexed with an octaose substrate.

spinqualitylabelsall models 5td4, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5td4 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: CA, CL, GLC, PCA, PRD_900001, PRD_900010, PRD_900035 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AMYP_HUMAN Publication Abstract from PubMed Starch provides the major source of caloric intake in many diets. Cleavage of starch into malto-oligosaccharides in the gut is catalyzed by pancreatic alpha-amylase. These oligosaccharides are then further cleaved by gut wall alpha-glucosidases to release glucose, which is absorbed into the bloodstream. Potential surface binding sites for starch on the pancreatic amylase, distinct from the active site of the amylase, have been identified through X-ray crystallographic analyses. The role of these sites in the degradation of both starch granules and soluble starch was probed by the generation of a series of surface variants modified at each site to disrupt binding. Kinetic analysis of the binding and/or cleavage of substrates ranging from simple maltotriosides to soluble starch and insoluble starch granules has allowed evaluation of the potential role of each such surface site. In this way, two key surface binding sites, on the same face as the active site, are identified. One site, containing a pair of aromatic residues, is responsible for attachment to starch granules, while a second site featuring a tryptophan residue around which a malto-oligosaccharide wraps is shown to heavily influence soluble starch binding and hydrolysis. These studies provide insights into the mechanisms by which enzymes tackle the degradation of largely insoluble polymers and also present some new approaches to the interrogation of the binding sites involved. Evaluation of the Significance of Starch Surface Binding Sites on Human Pancreatic alpha-Amylase.,Zhang X, Caner S, Kwan E, Li C, Brayer GD, Withers SG Biochemistry. 2016 Nov 1;55(43):6000-6009. Epub 2016 Oct 24. PMID:27756128 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Amylase 3D structures

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